EC number:1.1.1.3
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.1 Acting on the CH-OH group of donors |
| 1.1.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.1.1.3 |
|---|---|
| Description: | Homoserine dehydrogenase. |
| Prosite: | PDOC00800; |
| PDB: | |
| Cath: | 1.20.120.1320; 3.30.2130.10; 3.30.360.10; 3.30.70.260; 3.30.70.3100; 3.40.1160.10; 3.40.50.720; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.1.1.3 |
| BRENDA Enzyme Link: | BRENDA 1.1.1.3 |
| KEGG Enzyme Link: | KEGG1.1.1.3 |
| BioCyc Enzyme Link: | BioCyc 1.1.1.3 |
| ExPASy Enzyme Link: | ExPASy1.1.1.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.1.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.1.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.1.3 |
| IntEnz Enzyme Link: | IntEnz 1.1.1.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.1.3 |
| RHEA:15761 | L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde + NADPH |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[OH;+0:3].[*:4]-[n+;H0:5]1:[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:[c;H0;+0:9](-[*:10]):[cH;+0:11]:1>>[*:1]-[CH;+0:2]=[O;H0;+0:3].[*:4]-[N;H0;+0:5]1-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-[C;H0;+0:9](-[*:10])=[CH;+0:11]-1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain. | Véron M, Falcoz-Kelly F, Cohen GN | 1972 Aug 4 | 4562990 |
| Regulation of aspartate family amino acid biosynthesis in Brevibacterium flavum. 3. Properties of homoserine dehydrogenase. | Miyajima R, Shiio I | 1970 Sep | 4394351 |
| Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II. | Parsot C, Cohen GN | 1988 Oct 15 | 3139660 |
| A C-terminal deletion in Corynebacterium glutamicum homoserine dehydrogenase abolishes allosteric inhibition by L-threonine. | Archer JA, Solow-Cordero DE, Sinskey AJ | 1991 Oct 30 | 1743520 |
| Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms. Physiological context sets the specificity. | Curien G, Ravanel S, Robert M, Dumas R | 2005 Dec 16 | 16216875 |
| Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana. | Paris S, Wessel PM, Dumas R | 2002 Feb | 11812230 |
| RHEA:15757 | L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde + NADH |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[OH;+0:3].[*:4]-[n+;H0:5]1:[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:[c;H0;+0:9](-[*:10]):[cH;+0:11]:1>>[*:1]-[CH;+0:2]=[O;H0;+0:3].[*:4]-[N;H0;+0:5]1-[CH;+0:6]=[CH;+0:7]-[CH2;+0:8]-[C;H0;+0:9](-[*:10])=[CH;+0:11]-1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain. | Véron M, Falcoz-Kelly F, Cohen GN | 1972 Aug 4 | 4562990 |
| Regulation of aspartate family amino acid biosynthesis in Brevibacterium flavum. 3. Properties of homoserine dehydrogenase. | Miyajima R, Shiio I | 1970 Sep | 4394351 |
| Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II. | Parsot C, Cohen GN | 1988 Oct 15 | 3139660 |
| A C-terminal deletion in Corynebacterium glutamicum homoserine dehydrogenase abolishes allosteric inhibition by L-threonine. | Archer JA, Solow-Cordero DE, Sinskey AJ | 1991 Oct 30 | 1743520 |
| Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms. Physiological context sets the specificity. | Curien G, Ravanel S, Robert M, Dumas R | 2005 Dec 16 | 16216875 |
| Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana. | Paris S, Wessel PM, Dumas R | 2002 Feb | 11812230 |